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5 results for “advanced glycation end-products (AGE)”
Advanced Glycation End-products are Retained in Decellularized Muscle Matrix Derived from Aged Skeletal Muscle
<p>Advanced glycation end-products (AGEs) accrue on skeletal muscle collagen in old age, stiffening the matrix and increasing inflammation. Whether decellularized biomaterials derived from aged muscle would suffer from increased AGE cross-links is unknown. We hypothesized that DMM from old muscle would have increased collagen, collagen cross-linking, stiffness, and AGEs. We isolated, decellularized, and characterized gastrocnemii of 1-month, 2-month, and 20-month old C57BlJ6 mice to determine age-dependent changes to collagen in muscle and decellularized muscle matrix (DMM). Total hydroxyproline and soluble hydroxyproline after proteinase K digestion were measured to assay collagen levels and cross-linking, respectively. Muscle fiber and DMM stiffness was determined using atomic force microscopy (AFM). AGE ELISAs were used to test AGE levels, and the effect of AGE cross-link breaker ALT-711 on DMM was tested. We determined age-dependent increases in collagen amount, cross-linking, and general stiffness are retained on DMM. DMM from old muscle was stiffer compared to younger groups according to shifts in AFM modulus distribution. We measured an increase in AGE-specific cross-links with old age in whole muscle and observed that these changes are countered in DMM by AGE cross-link breaker ALT-711. Future study investigating and countering the biological effects of old age on DMM is warranted.</p>
Evaluation of Advanced Glycation End-products (AGE) and the Erectile Dysfunction (DE) in Diabetic Patients
ClinicalTrials.gov study NCT02770235. IPD Sharing: Not stated. Countries: 1. Publications: 1.
A Low AGE (Advanced Glycation End-product) Dietary Intervention for Breast Cancer Survivors
ClinicalTrials.gov study NCT05265715. IPD Sharing: YES. Countries: 1. Publications: 0.
Soluble Receptor for Advanced Glycation End-products regulates age-associated Cardiac Fibrosis
<p>This record contains raw data related to the article "Soluble Receptor for Advanced Glycation End-products regulates age-associated Cardiac Fibrosis"</p> <p>Myocardial aging increases the cardiovascular risk in the elderly. The Receptor for Advanced Glycation End-products (RAGE) is involved in age-related disorders. The soluble isoform (sRAGE) acts as a scavenger blocking the membrane-bound receptor activation. This study aims at investigating RAGE contribution to age-related cardiac remodeling. We analyzed the cardiac function of three different age groups of female <em>Rage-/-</em> and C57BL/6N (WT) mice: 2.5- (Young), 12- (Middle-age, MA) and 21-months (Old) old. While aging, <em>Rage-/-</em> mice displayed an increase in left ventricle (LV) dimensions compared to age-matched WT animals, with the main differences observed in the MA groups. <em>Rage-/-</em> mice showed higher fibrosis and a larger number of α-Smooth Muscle Actin (SMA)+ cells with age, along with increased expression of pro-fibrotic Transforming Growth Factor (TGF)-β1 pathway components. RAGE isoforms were undetectable in LV of WT mice, nevertheless, circulating sRAGE declined with aging and inversely associated with LV diastolic dimensions. Human cardiac fibroblasts stimulated with sRAGE exhibited a reduction in proliferation, pro-fibrotic proteins and TGF-beta Receptor 1 (TGFbR1) expression and Smad2-3 activation. Finally, sRAGE administration to MA WT animals reduced cardiac fibrosis. Hence, our work shows that RAGE associates with age-dependent myocardial changes and indicates sRAGE as an inhibitor of cardiac fibroblasts differentiation and age-dependent cardiac fibrosis.</p>
Dataset related to the article "Modulation of soluble receptor for advanced glycation end-products (RAGE) isoforms and their ligands in healthy aging"
<p>This record contains raw data related to the article "Modulation of soluble receptor for advanced glycation end-products (RAGE) isoforms and their ligands in healthy aging" </p> <p> The receptor for advanced glycation end-products (RAGE) recognizes several ligands involved in inflammatory diseases. Two circulating soluble isoforms exist: esRAGE derived from alternative splicing and cRAGE generated by the membrane-bound RAGE (FL-RAGE) proteolysis. Together, esRAGE and cRAGE constitute sRAGE and function as decoy receptors preventing FL-RAGE/ligands binding.</p> <p>We determined serum concentration of both, esRAGE and cRAGE, and their ligands AGEs, HMGB1 and S100A8/A9 in a healthy population of 169 subjects aged 20-90 years. cRAGE showed a negative (r=-0.375, P<0.0001) while AGEs (r=0.160, P=0.0384) and S100A8/A9 (r=0.207, P=0.0091) a positive correlation with age. esRAGE did not change during aging and inversely correlated with Hemoglobin, ALT, insulin, HOMA index, Waist-Hip ratio (W/H), Waist Circumference (WC) and positively with AGEs. cRAGE exhibited also an inverse correlation with WC, W/H, PAI-1, HMGB1, AGEs and S100A8/A9. Age, W/H, HMGB1, S100A8/A9 and AGEs are independent predictors of cRAGE, whereas W/H and AGEs associate with esRAGE. Treatment of cells with glycated albumin reduced cRAGE production and upregulated FL-RAGE<em>. </em></p> <p>These results indicate that in a healthy population cRAGE is a biomarker of aging while esRAGE represents a more reliable marker of obesity and insulin resistance. Hence, sRAGE isoforms levels could be differentially associated with age-related diseases risk factors.</p>
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